Q7LZ71 (IXA_PROFL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Coagulation factor IX-binding protein subunit A Short name=IX-bp A
Organism	Protobothrops flavoviridis (Habu) (Trimeresurus flavoviridis)
Taxonomic identifier	88087 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Viperidae › Crotalinae › Trimeresurus

Protein attributes

Sequence length	129 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Anticoagulant protein which binds to the gamma-carboxyglutamic acid-domain regions of factor IX (but not factor X) in the presence of calcium with a 1 to 1 stoichiometry.
Subunit structure	Heterodimer of subunits A and B; disulfide-linked. Ref.2 Ref.3 Ref.4
Subcellular location	Secreted.
Tissue specificity	Expressed by the venom gland.
Sequence similarities	Contains 1 C-type lectin domain.

Ontologies

Keywords
Biological process	Blood coagulation
Cellular component	Secreted
Ligand	Calcium Lectin Metal-binding
Molecular function	Toxin
PTM	Disulfide bond
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	blood coagulation Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW sugar binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 129

129

Coagulation factor IX-binding protein subunit A

PRO_0000346754

Regions

Domain

1 – 129

129

C-type lectin

Sites

Metal binding

41

1

Calcium; via carbonyl oxygen

Metal binding

43

1

Calcium

Metal binding

47

1

Calcium

Metal binding

128

1

Calcium

Amino acid modifications

Disulfide bond

2 ↔ 13

Ref.2 Ref.3 Ref.4

Disulfide bond

30 ↔ 127

Ref.2 Ref.3 Ref.4

Disulfide bond

79

Interchain (with C-98 in subunit B) Ref.2 Ref.3 Ref.4

Disulfide bond

102 ↔ 119

Ref.2 Ref.3 Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

129

Helix Strand Turn

Details...

Beta strand

7 – 9

3

Beta strand

12 – 21

10

Helix

23 – 31

9

Helix

45 – 58

14

Beta strand

66 – 74

9

Helix

96 – 98

3

Beta strand

102 – 105

4

Helix

107 – 109

3

Beta strand

113 – 117

5

Sequences

	Sequence		Length	Mass (Da)
	Q7LZ71 [UniParc]. Last modified December 15, 2003. Version 1. Checksum: 225F3C7D841D8C76	FASTA	129	14,640
	10 20 30 40 50 60 DCPSGWSSYE GHCYKPFKLY KTWDDAERFC TEQAKGGHLV SIESAGEADF VAQLVTENIQ 70 80 90 100 110 120 NTKSYVWIGL RVQGKEKQCS SEWSDGSSVS YENWIEAESK TCLGLEKETG FRKWVNIYCG QQNPFVCEA

References

[1]	"Blood coagulation factor IX-binding protein from the venom of Trimeresurus flavoviridis: purification and characterization." Atoda H., Ishikawa M., Yoshihara E., Sekiya F., Morita T. J. Biochem. 118:965-973(1995) [PubMed: 8749314] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Venom.
[2]	"Crystal structure of coagulation factor IX-binding protein from habu snake venom at 2.6 A: implication of central loop swapping based on deletion in the linker region." Mizuno H., Fujimoto Z., Koizumi M., Kano H., Atoda H., Morita T. J. Mol. Biol. 289:103-112(1999) [PubMed: 10339409] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), METAL-BINDING SITES, DISULFIDE BONDS. Tissue: Venom.
[3]	"Crystal structure of Mg2+- and Ca2+-bound Gla domain of factor IX complexed with binding protein." Shikamoto Y., Morita T., Fujimoto Z., Mizuno H. J. Biol. Chem. 278:24090-24094(2003) [PubMed: 12695512] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS), METAL-BINDING SITES, DISULFIDE BONDS. Tissue: Venom.
[4]	"pH-dependent structural changes at Ca(2+)-binding sites of coagulation factor IX-binding protein." Suzuki N., Fujimoto Z., Morita T., Fukamizu A., Mizuno H. J. Mol. Biol. 353:80-87(2005) [PubMed: 16165155] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS), METAL-BINDING SITES, DISULFIDE BONDS. Tissue: Venom.
+	Additional computationally mapped references.

Cross-references

Sequence databases

PIR

JC4329.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BJ3	X-ray	2.60	A	1-129	[»]
1J34	X-ray	1.55	A	1-129	[»]
1J35	X-ray	1.80	A	1-129	[»]
1X2T	X-ray	1.72	A/C	1-129	[»]
1X2W	X-ray	2.29	A	1-129	[»]

ProteinModelPortal

Q7LZ71.

SMR

Q7LZ71. Positions 1-129.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Phylogenomic databases

HOVERGEN

HBG004151.

Family and domain databases

InterPro

IPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_fold.
[Graphical view]

Gene3D

G3DSA:3.10.100.10. C-type_lectin-like. 1 hit.

Pfam

PF00059. Lectin_C. 1 hit.
[Graphical view]

SMART

SM00034. CLECT. 1 hit.
[Graphical view]

SUPFAM

SSF56436. C-type_lectin_fold. 1 hit.

PROSITE

PS00615. C_TYPE_LECTIN_1. 1 hit.
PS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

IXA_PROFL

Accession

Primary (citable) accession number: Q7LZ71

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 2, 2008
Last sequence update:	December 15, 2003
Last modified:	September 21, 2011
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Annotation program

Animal Toxin Annotation Program